3c0r: Difference between revisions

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[[Image:3c0r.png|left|200px]]
{{STRUCTURE_3c0r|  PDB=3c0r  |  SCENE=  }}  
{{STRUCTURE_3c0r|  PDB=3c0r  |  SCENE=  }}  
===Structure of Ovarian Tumor (OTU) domain in complex with Ubiquitin===
===Structure of Ovarian Tumor (OTU) domain in complex with Ubiquitin===
{{ABSTRACT_PUBMED_18270205}}


{{ABSTRACT_PUBMED_18270205}}
==Function==
[[http://www.uniprot.org/uniprot/OTU1_YEAST OTU1_YEAST]] Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Participates in the regulation of the ubiquin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May be indireclty involved in PIS1 gene expression.<ref>PMID:15755922</ref> <ref>PMID:16427015</ref> 


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:018270205</ref><references group="xtra"/>
<ref group="xtra">PMID:018270205</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]

Revision as of 14:19, 3 July 2013

Template:STRUCTURE 3c0r

Structure of Ovarian Tumor (OTU) domain in complex with UbiquitinStructure of Ovarian Tumor (OTU) domain in complex with Ubiquitin

Template:ABSTRACT PUBMED 18270205

FunctionFunction

[OTU1_YEAST] Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Participates in the regulation of the ubiquin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May be indireclty involved in PIS1 gene expression.[1] [2]

About this StructureAbout this Structure

3c0r is a 4 chain structure with sequence from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Messick TE, Russell NS, Iwata AJ, Sarachan KL, Shiekhattar R, Shanks JR, Reyes-Turcu FE, Wilkinson KD, Marmorstein R. Structural basis for ubiquitin recognition by the Otu1 ovarian tumor domain protein. J Biol Chem. 2008 Apr 18;283(16):11038-49. Epub 2008 Feb 12. PMID:18270205 doi:http://dx.doi.org/10.1074/jbc.M704398200
  1. Gardocki ME, Bakewell M, Kamath D, Robinson K, Borovicka K, Lopes JM. Genomic analysis of PIS1 gene expression. Eukaryot Cell. 2005 Mar;4(3):604-14. PMID:15755922 doi:10.1128/EC.4.3.604-614.2005
  2. Rumpf S, Jentsch S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell. 2006 Jan 20;21(2):261-9. PMID:16427015 doi:S1097-2765(05)01897-6

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